O‐linked protein glycosylation in mycoplasma. Issue 5 (18th October 2013)

• Record Type: Journal Article
• Authors: Jordan, David S.; Daubenspeck, James M.; Laube, Audra H.; Renfrow, Matthew B.; Dybvig, Kevin
• Is Part Of: Molecular microbiology. Volume 90:Issue 5(2013)
• Page Start: 1046
• Page End: 1053
• Publication Date: 2013-10-18
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.12415
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>Although mycoplasmas have a paucity of glycosyltransferases and nucleotidyltransferases recognizable by bioinformatics, these bacteria are known to produce polysaccharides and glycolipids. We show here that mycoplasmas also produce glycoproteins and hence have glycomes more complex than previously realized. Proteins from several species of <italic>Mycoplasma</italic> reacted with a glycoprotein stain, and the murine pathogen <italic>Mycoplasma arthritidis</italic> was chosen for further study. The presence of <italic>M. arthritidis</italic> glycoproteins was confirmed by high‐resolution mass spectrometry. <italic>O</italic>‐linked glycosylation was clearly identified at both serine and threonine residues. No consensus amino acid sequence was evident for the glycosylation sites of the glycoproteins. A single hexose was identified as the <italic>O</italic>‐linked modification, and glucose was inferred by ¹³C‐labelling to be the hexose at several of the glycosylation sites. This is the first study to conclusively identify sites of protein glycosylation in any of the mollicutes.</p> </abstract>